title: Noroviral P particle: structure, function and applications in virus-host interaction.
abstract: Noroviruses are an important cause of epidemic acute gastroenteritis and the viruses recognize human histo-blood group antigens (HBGAs) as receptors. The protruding (P) domain of noroviral capsid, the receptor-binding domain, forms subviral particles in vitro that retain the receptor-binding function. In this study we characterized the structure and HBGA-binding function of the P particle. Structure reconstruction using cryo-EM showed that the P particles are comprised of 12 P dimers that are organized in octahedral symmetry. The dimeric packing of the proteins in the P particles is similar to that in the norovirus capsid, in which the P2 subdomain with the receptor-binding interface is located at the outermost surface of the P particle. The P particles are immunogenic and reveal similar antigenic and HBGA-binding profiles with their parental virus-like particle, further confirming the shared surface structures between the two types of particles. The P particles are easily produced in E. coli and yeast and are stable, which are potentially useful for a broad application including vaccine development against noroviruses.
authors.affiliation: Division of Infectious Diseases, Cincinnati Children's Hospital Medical Center, 3333 Burnet Avenue, Cincinnati, OH 45229-3039, USA.
authors.forename: Ming
authors.initials: M
authors.lastname: Tan
authors.forename: Pingan
authors.initials: P
authors.lastname: Fang
authors.forename: Teepanis
authors.initials: T
authors.lastname: Chachiyo
authors.forename: Ming
authors.initials: M
authors.lastname: Xia
authors.forename: Pengwei
authors.initials: P
authors.lastname: Huang
authors.forename: Zhaoyin
authors.initials: Z
authors.lastname: Fang
authors.forename: Wen
authors.initials: W
authors.lastname: Jiang
authors.forename: Xi
authors.initials: X
authors.lastname: Jiang
mesh_terms: D000818:Animals; D001665:Binding Sites; D036022:Capsid Proteins / Q000276:immunology / Q000378:metabolism* / Q000648:ultrastructure*; D020285:Cryoelectron Microscopy; D019281:Dimerization; D004926:Escherichia coli / Q000235:genetics; D046911:Macromolecular Substances / Q000276:immunology / Q000378:metabolism*; D051379:Mice; D008958:Models, Molecular; D029322:Norovirus / Q000648:ultrastructure*; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D011991:Receptors, Virus / Q000378:metabolism; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics; D012440:Saccharomyces / Q000235:genetics; D022701:Virosomes / Q000276:immunology / Q000378:metabolism*
chemical_list: D036022:Capsid Proteins; D046911:Macromolecular Substances; D011991:Receptors, Virus; D011994:Recombinant Proteins; D022701:Virosomes